JKK1_CAEEL
ID JKK1_CAEEL Reviewed; 435 AA.
AC G5EDT6;
DT 22-JUL-2015, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Dual specificity mitogen-activated protein kinase kinase jkk-1 {ECO:0000305};
DE Short=MAP kinase kinase jkk-1 {ECO:0000305};
DE EC=2.7.12.2 {ECO:0000269|PubMed:10393177};
DE AltName: Full=JNK-1 activator kinase {ECO:0000303|PubMed:10393177};
DE Short=JNK kinase {ECO:0000312|WormBase:F35C8.3};
GN Name=jkk-1 {ECO:0000312|WormBase:F35C8.3};
GN ORFNames=F35C8.3 {ECO:0000312|WormBase:F35C8.3};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|EMBL:BAA82641.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF LYS-149.
RX PubMed=10393177; DOI=10.1093/emboj/18.13.3604;
RA Kawasaki M., Hisamoto N., Iino Y., Yamamoto M., Ninomiya-Tsuji J.,
RA Matsumoto K.;
RT "A Caenorhabditis elegans JNK signal transduction pathway regulates
RT coordinated movement via type-D GABAergic motor neurons.";
RL EMBO J. 18:3604-3615(1999).
RN [2] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3] {ECO:0000305}
RP FUNCTION, AND INTERACTION WITH UNC-16.
RX PubMed=11738026; DOI=10.1016/s0896-6273(01)00532-3;
RA Byrd D.T., Kawasaki M., Walcoff M., Hisamoto N., Matsumoto K., Jin Y.;
RT "UNC-16, a JNK-signaling scaffold protein, regulates vesicle transport in
RT C. elegans.";
RL Neuron 32:787-800(2001).
RN [4] {ECO:0000305}
RP FUNCTION.
RX PubMed=15767565; DOI=10.1073/pnas.0500749102;
RA Oh S.W., Mukhopadhyay A., Svrzikapa N., Jiang F., Davis R.J.,
RA Tissenbaum H.A.;
RT "JNK regulates lifespan in Caenorhabditis elegans by modulating nuclear
RT translocation of forkhead transcription factor/DAF-16.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:4494-4499(2005).
RN [5] {ECO:0000305}
RP FUNCTION.
RX PubMed=18597494; DOI=10.1021/tx800074e;
RA Pei B., Wang S., Guo X., Wang J., Yang G., Hang H., Wu L.;
RT "Arsenite-induced germline apoptosis through a MAPK-dependent, p53-
RT independent pathway in Caenorhabditis elegans.";
RL Chem. Res. Toxicol. 21:1530-1535(2008).
RN [6] {ECO:0000305}
RP FUNCTION.
RX PubMed=17894411; DOI=10.1002/jcp.21269;
RA Wolf M., Nunes F., Henkel A., Heinick A., Paul R.J.;
RT "The MAP kinase JNK-1 of Caenorhabditis elegans: location, activation, and
RT influences over temperature-dependent insulin-like signaling, stress
RT responses, and fitness.";
RL J. Cell. Physiol. 214:721-729(2008).
RN [7] {ECO:0000305}
RP FUNCTION.
RX PubMed=19497412; DOI=10.1016/j.cbi.2009.03.012;
RA Wang S., Wu L., Wang Y., Luo X., Lu Y.;
RT "Copper-induced germline apoptosis in Caenorhabditis elegans: the
RT independent roles of DNA damage response signaling and the dependent roles
RT of MAPK cascades.";
RL Chem. Biol. Interact. 180:151-157(2009).
CC -!- FUNCTION: Dual specificity protein kinase which acts as an essential
CC component of the JNK signal transduction pathway. May phosphorylate
CC jnk-1 (PubMed:10393177, PubMed:15767565, PubMed:17894411). Plays a role
CC in coordinating locomotion via D-type GABAergic motoneurons and in
CC regulating synaptic vesicle transport downstream of adapter protein
CC unc-16 and probably by activating jnk-1 (PubMed:10393177,
CC PubMed:11738026). Positively regulates lifespan (PubMed:15767565). Upon
CC environmental stress such as heat stress regulates daf-16 nuclear
CC translocation probably by activating jnk-1 (PubMed:15767565). Regulates
CC germline cell apoptosis in response to heavy metals such as Cu(2+) and
CC to arsenite (PubMed:18597494, PubMed:19497412).
CC {ECO:0000269|PubMed:10393177, ECO:0000269|PubMed:11738026,
CC ECO:0000269|PubMed:15767565, ECO:0000269|PubMed:17894411,
CC ECO:0000269|PubMed:18597494, ECO:0000269|PubMed:19497412}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.12.2;
CC Evidence={ECO:0000269|PubMed:10393177};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.12.2; Evidence={ECO:0000269|PubMed:10393177};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.12.2;
CC Evidence={ECO:0000269|PubMed:10393177};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:O14733};
CC -!- SUBUNIT: Interacts with unc-16. {ECO:0000269|PubMed:11738026}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10393177}.
CC Perikaryon {ECO:0000269|PubMed:10393177}. Cell projection, axon
CC {ECO:0000269|PubMed:10393177}.
CC -!- TISSUE SPECIFICITY: Expressed in most neurons, including nerve ring,
CC head ganglions, dorsal and ventral nerve cords and tail ganglions.
CC {ECO:0000269|PubMed:10393177}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. MAP kinase kinase subfamily. {ECO:0000305}.
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DR EMBL; AB024086; BAA82641.1; -; mRNA.
DR EMBL; BX284606; CCD62782.1; -; Genomic_DNA.
DR PIR; T16256; T16256.
DR PIR; T37324; T37324.
DR RefSeq; NP_508913.1; NM_076512.4.
DR AlphaFoldDB; G5EDT6; -.
DR SMR; G5EDT6; -.
DR IntAct; G5EDT6; 6.
DR STRING; 6239.F35C8.3; -.
DR PaxDb; G5EDT6; -.
DR EnsemblMetazoa; F35C8.3.1; F35C8.3.1; WBGene00002177.
DR EnsemblMetazoa; F35C8.3.2; F35C8.3.2; WBGene00002177.
DR GeneID; 180810; -.
DR CTD; 180810; -.
DR WormBase; F35C8.3; CE24941; WBGene00002177; jkk-1.
DR eggNOG; KOG0983; Eukaryota.
DR HOGENOM; CLU_000288_63_23_1; -.
DR InParanoid; G5EDT6; -.
DR OMA; KICMQIM; -.
DR OrthoDB; 688282at2759; -.
DR PhylomeDB; G5EDT6; -.
DR SignaLink; G5EDT6; -.
DR PRO; PR:G5EDT6; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00002177; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0030424; C:axon; IDA:WormBase.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0043025; C:neuronal cell body; IDA:WormBase.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004527; F:exonuclease activity; ISS:WormBase.
DR GO; GO:0008545; F:JUN kinase kinase activity; IMP:WormBase.
DR GO; GO:0004708; F:MAP kinase kinase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0006972; P:hyperosmotic response; IGI:WormBase.
DR GO; GO:0040011; P:locomotion; IMP:WormBase.
DR GO; GO:0000165; P:MAPK cascade; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IMP:WormBase.
DR GO; GO:0051403; P:stress-activated MAPK cascade; IBA:GO_Central.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell projection; Cytoplasm; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Reference proteome; Serine/threonine-protein kinase;
KW Stress response; Transferase; Tyrosine-protein kinase.
FT CHAIN 1..435
FT /note="Dual specificity mitogen-activated protein kinase
FT kinase jkk-1"
FT /evidence="ECO:0000305"
FT /id="PRO_0000433602"
FT DOMAIN 122..385
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 35..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..66
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 246
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 128..136
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 149
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MUTAGEN 149
FT /note="K->R: Loss of kinase activity."
FT /evidence="ECO:0000269|PubMed:10393177"
SQ SEQUENCE 435 AA; 50014 MW; 71C2D899A6719CEA CRC64;
MENVCFQQRL RDLETRVRKW KFLKLGLTEV RLRPRDRRST SVDQKHKECS STSSSPQHQR
PNNIGYLTSP MERKFTPLSM KPSPSRRDTE KDALEYEFLE GYKKSGTLEI DGEKQVVDPN
EIHIISLLGS GSCGVVESAT VRSKLMAVKT MYKNDNKENL KRILRDVRIM SMCNSPFIVT
SYGYFMFDSS VKICMQIMSA CCEKLLRRIY HSKLDFFPEF VAGHIVYSAI SALDYLKEKH
SIIHRDIKPS NILFDDSGNV KLCDFGISGF MTDSMAHSKS AGCPPYMAPE RLTIETNSKY
DVRSDVWSLG ITVYQLVTGL YPFPLNDMEF TTLTIIANLN LPSPSLREET KRSFSPLFIE
FLDLCLRKDV RERPEYRQLM KHDFYLDYDP ASGSAYKFKA INGKCNQVAD WFVDVIRLSK
TEDELKSIPN TPCVN
